Application | Comment | Organism |
---|---|---|
pharmacology | the structure of HemN sets the stage for the development of inhibitors with antibacterial function due to the uniquely bacterial occurence of the enzyme | Escherichia coli |
Cloned (Comment) | Organism |
---|---|
- |
Escherichia coli |
Crystallization (Comment) | Organism |
---|---|
crystal structure, co-crystallized with S-adenosyl-L-methionine, hanging-drop vapor diffusion method, X-ray analysis | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
coproporphyrinogen-III + S-adenosyl-L-methionine | Escherichia coli | HemN catalyzes the essential conversion of coproporphyrinogen-III to protoporphyrinogen IX during heme biosynthesis | protoporphyrinogen IX + CO2 + L-methionine + 5'-deoxyadenosine | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P32131 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant HemN | Escherichia coli |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
coproporphyrinogen III + 2 S-adenosyl-L-methionine = protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine | mechanism | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
coproporphyrinogen-III + S-adenosyl-L-methionine | HemN catalyzes the essential conversion of coproporphyrinogen-III to protoporphyrinogen IX during heme biosynthesis | Escherichia coli | protoporphyrinogen IX + CO2 + L-methionine + 5'-deoxyadenosine | - |
? | |
coproporphyrinogen-III + S-adenosyl-L-methionine | mechanism, the S-adenosyl-L-methionine sulfonium sulfur is near both the Fe and neighboring sulfur of the cluster allowing single electron transfer from the 4Fe-4S cluster to the S-adenosyl-L-methionine sulfonium. S-adenosyl-L-methionine is cleaved yielding a highly oxidizing 5-deoxyadenosyl radical, HemN binds a second S-adenosyl-L-methionine immediately adjacent to the first and may thus successively catalyze two propionate decarboxylations. Cofactor geometry required for Radical SAM catalysis, detailed enzyme structure, two distinct domains, domain structure, S-adenosyl-L-methionine binding mode | Escherichia coli | protoporphyrinogen IX + CO2 + L-methionine + 5'-deoxyadenosine | - |
? |
Subunits | Comment | Organism |
---|---|---|
monomer | monomeric enzyme consisting of two distinct domains | Escherichia coli |
Synonyms | Comment | Organism |
---|---|---|
More | belongs to the Radical SAM protein family | Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
4Fe-4S-center | HemN binds a 4Fe-4S cluster through three cysteine residues: Cys-62, Cys-66 and Cys-69, a juxtaposed S-adenosyl-L-methionine coordinates the fourth Fe ion through its amide nitrogen and carboxylate oxygen, detailed binding mode, cofactor geometry required for Radical SAM catalysis | Escherichia coli | |
S-adenosyl-L-methionine | HemN contains two S-adenosyl-L-methionine molecules as cofactors, detailed binding mode | Escherichia coli |